2HDN
Trypsin-modified Elongation Factor Tu in complex with tetracycline at 2.8 Angstrom resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU |
Temperature [K] | 298 |
Detector technology | AREA DETECTOR |
Detector | SDMS |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 69.710, 156.060, 134.830 |
Unit cell angles | 90.00, 95.38, 90.00 |
Refinement procedure
Resolution | 40.000 - 2.800 |
Rwork | 0.180 |
R-free | 0.22300 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | an unrefined 2.7 Angstrom model of E. coli trypsin-modified EF-Tu-MgGDP consisting of residues 9 to 40 50 to 258 and 260 to 393 plus one Mg ion and GDP |
RMSD bond length | 0.020 |
RMSD bond angle | 1.820 |
Phasing software | MERLOT |
Refinement software | CNS |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 47.300 |
High resolution limit [Å] | 2.700 |
Rmerge | 0.099 |
Number of reflections | 73085 |
Completeness [%] | 92.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | Multiple crystals were used to collect the native and each derivative data set. VAPOR DIFFUSION, SITTING DROP |